User:Jiaming Zhuang/Sandbox 2: Difference between revisions

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<applet size='[450,338]' frame='true' align='right'
<Structure load='1gkc' size='400' frame='true' align='right' caption='MMP9' scene='Insert optional scene name here' />
caption='YYY' />


<scene name='User:Jiaming_Zhuang/Sandbox_2/Mmp-12/1'>TextToBeDisplayed</scene> The catalytic domain of human MMP12 complexed with the inhibitor (R)-2-(biphenyl-4-ylsulfonamido)-4-methylpentanoic acid
MMP9 is a member of ''' matrix metalloproteinases''' (MMPs) which are zinc-dependent endopeptidases. It has been found to associate with many types of cancers and investigated as a potential drug target. Various of <scene name='User:Jiaming_Zhuang/Sandbox_2/Ligand/1'>inhibitors</scene> have been designed to bind to the <scene name='User:Jiaming_Zhuang/Sandbox_2/Domain1/1'>catalytic domain</scene> and inhibit the activity of MMP9.
 
 
ProMMP9 has a propeptide domain with a zinc ligating "cysteine switch" at the <scene name='40/400553/Pro_cat_motif/4'>active site</scene>, rendering the enzyme inactive until the propeptide is cleaved.
 
 
 
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Reference:
Siân Rowsell, Paul Hawtin,Claire A. Minshull, Holly Jepson, Sarah M.V. Brockbank,Derek G. Barratt, Anthony M. Slater, William L. McPheat, David Waterson, Adriano M. Henney, Richard A. Pauptit Crystal Structure of Human MMP9 in Complex with a Reverse Hydroxamate Inhibitor, Volume 319, Issue 1, 24 May 2002, Pages 173–181
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